Abstract
In the field of tissue engineering, recombinant protein-based biomaterials made up of block polypeptides with tunable properties arising from the functionalities of the individual domains are appealing candidates for the construction of medical devices. In this work, we focused our attention on the preparation and structural characterization of nanofibers from a chimeric-polypeptide-containing resilin and elastin domain, designed on purpose to enhance its cell-binding ability by introducing a specific fibronectin-derived Arg-Gly-Asp (RGD) sequence. The polypeptide ability to self-assemble was investigated. The molecular and supramolecular structure was characterized by Scanning Electronic Microscopy (SEM) and Atomic Force Microscopy (AFM), circular dichroism, state-of-the-art synchrotron radiation-induced techniques X-ray photoelectron spectroscopy (XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS). The attained complementary results allow us to assess as H-bonds influence the morphology of the aggregates obtained after the self-assembling of the chimeric polypeptide. Finally, a preliminary investigation of the potential cytotoxicity of the polypeptide was performed by culturing human fetal foreskin fibroblast (HFFF2) for its use as biomedical device.
Highlights
In the research framework of tissue engineering, recombinant protein-based biomaterials are promising candidates for the construction of medical devices
We focused our attention on the preparation and structural characterization of nanofibers from a chimeric-polypeptide-containing resilin and elastin domain, designed on purpose to enhance its cell-binding ability by introducing a specific fibronectin-derived Arg-Gly-Asp (RGD) sequence
The polypeptide ability to self-assemble was demonstrated by means of turbidimetric assays
Summary
In the research framework of tissue engineering, recombinant protein-based biomaterials are promising candidates for the construction of medical devices. The biopolymers are composed of block polypeptides combined by ligation of genes encoding polypeptide sequences inspired by different proteins with tunable properties conferred by each block domain. The chimera could be made of different proteins, such as elastin, resilin, and collagen (REC)-inspired sequences [1]. Elastin-inspired sequences have been widely employed both in structural studies aimed to elucidate the mechanism of elasticity of the protein and in recombinant engineered polypeptides [3,4], while resilin-like polypeptides were less investigated [5]. A recombinant resilin/elastin-like diblock copolypeptide having sequences different from those used in the present work were produced in a recent paper from Chilkoti and co-workers [13,14]. The diblock copolypeptides exhibited both lower and upper critical solution temperature phase behavior according to the length of the resilin- or elastin-mimetic blocks and self-assembled into spherical or cylindrical micelles
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